Alweera Ashfaq, Asma Ibrahim AlKhanbashi, Bincy Bhaskar, Pei-Gee Yap, Masataka Wakayama, Tatsuki Ogura, Abdul Raziq Kakar, Gan Chee Yuen, Priti Mudgil, Sajid Maqsood
Camel colostrum is the least studied source of dairy protein that could yield high-quality bioactive peptides with hypocholesterolaemic activity. Therefore, we comparatively investigated anti-hypercholesterolemic activity of hydrolysates generated from camel colostrum (CC) and mature camel milk (MCM) using alcalase (A2-6), flavorzyme (F2-6), and neutrase (N2-6). Results showed Alcalase as the most effective enzyme for hydrolyzing CC and MCM proteins, outperforming flavorzyme and neutrase as evidenced by its higher free amino nitrogen (FAN) content. Overall, camel colostrum hydrolysates (CCHs) demonstrated better Pancreatic lipase (PL) inhibitory effects compared with their corresponding mature camel milk hydrolysates (MCMHs). For PL inhibition, the IC50 values of CCHs are lower (IC50A6: 27.43 ± 0.68, F6: 44.15 ± 4.8, and N6: 40.78 ± 2.64) than MCMHs (IC50: A6: 36.08 ± 0.91, F6: 74.52 ± 12.7, and N6: 56.7 ± 15.39). However, Cholesterol esterase (CE) inhibitory effects (IC50: A631.81 ± 1.71, F6: 46.94 ± 2.89, N6; 46.63 ± 4.5) of CCH were higher in all cases except F6: 74.52 ± 12.7 and N6: 56.7 ± 15.39 compared with MCMHs with F6: 70.77 ± 8.65 and N6: 53.32 ± 2.6. Molecular docking revealed that identified peptides disrupt PL and CE enzyme-substrate interactions by binding at hotspot sites and distant residues. Peptides, LHPVPQPLVPVI and PQPVPQTPMIPPQSL, were predicted to act as both PL and CE inhibitors, warranting future research via peptide synthesis or in vivo studies. Metabolomics also confirmed diverse post-hydrolysis metabolites, positioning CCHs as promising nutraceuticals for obesity and well-being.